Name
Abstract | ||
|---|---|---|
Currently the protein mutant database (PMD) contains over 81 000 mutants, including artificial as well as natural mutants of various proteins extracted from about 10 000 articles. We recently developed a powerful viewing and retrieving system (http://pmd.ddbj.nig.ac.jp), which is integrated with the sequence and tertiary structure databases. The system has the following features: (i) mutated sequences are displayed after being automatically generated from the information described in the entry together with the sequence data of wild-type proteins integrated. This is a convenient feature because it allows one to see the position of altered amino acids (shown in a different color) in the entire sequence of a wild-type protein; (ii) for those proteins whose 3D structures have been experimentally determined, a 3D structure is displayed to show mutation sites in a different color; (iii) a sequence homology search against PMD can be carried out with any query sequence; (iv) a summary of mutations of homologous sequences can be displayed, which shows all the mutations at a certain site of a protein, recorded throughout the PMD. |
Year | DOI | Venue |
|---|---|---|
1999 | 10.1093/nar/27.1.355 | NUCLEIC ACIDS RESEARCH |
Keywords | Field | DocType |
amino acids,mutation,internet,amino acid sequence,protein conformation,proteins,sequence alignment | Conserved sequence,Sequence logo,Sequence database,Protein tertiary structure,Biology,Threading (protein sequence),Multiple sequence alignment,Genetics,Homology modeling,Database,Sequence analysis | Journal |
Volume | Issue | ISSN |
27 | 1 | 0305-1048 |
Citations | PageRank | References |
40 | 2.75 | 1 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Takeshi Kawabata | 1 | 296 | 51.73 |
| Motonori Ota | 2 | 135 | 29.12 |
| K Nishikawa | 3 | 82 | 9.53 |